RNA-protein interactions

Curr Opin Struct Biol. 2002 Jun;12(3):283-8. doi: 10.1016/s0959-440x(02)00323-8.

Abstract

Recent discoveries have revealed that there is a myriad of RNAs and associated RNA-binding proteins that spatially and temporally appear in the cells of all organisms. The structures of these RNA-protein complexes are providing valuable insights into the binding modes and functional implications of these interactions. Even the common RNA-binding domains (RBDs) and the double stranded RNA binding motifs (dsRBMs) have been shown to exhibit a plethora of binding modes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Deaminase / metabolism
  • ELAV Proteins
  • Helminth Proteins / metabolism
  • Humans
  • Muscle Proteins / metabolism
  • Nerve Tissue Proteins / metabolism
  • Nuclear Cap-Binding Protein Complex / metabolism
  • Nuclear Proteins*
  • Nucleolin
  • Phosphoproteins / metabolism
  • Polypyrimidine Tract-Binding Protein / metabolism
  • Protein Binding
  • RNA / metabolism*
  • RNA-Binding Proteins / metabolism*
  • Ribonucleoproteins / metabolism
  • Splicing Factor U2AF
  • eIF-2 Kinase / metabolism

Substances

  • ELAV Proteins
  • Helminth Proteins
  • Muscle Proteins
  • Nerve Tissue Proteins
  • Nuclear Cap-Binding Protein Complex
  • Nuclear Proteins
  • Phosphoproteins
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • Splicing Factor U2AF
  • U2AF1 protein, human
  • calponin homolog protein, Schistosoma japonicum
  • Polypyrimidine Tract-Binding Protein
  • RNA
  • eIF-2 Kinase
  • Adenosine Deaminase